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Research Article

Structure and Dynamics of Serine Hydrolase-Organophosphate Adducts

Pages 199-208 | Received 24 Oct 1987, Published online: 27 Sep 2008
 

Abstract

The structural profile for the interactions between serine proteases and organophosphorus (OP) compounds can be deduced from recent NMR and X-ray crystallographic data. Using the rationale proposed for serine proteases, dynamic data on the inhibition of acetylcholinesterase by OP compounds is also consistent with structural constraints and an impairment of the proton switch mechanism during phosphylation.

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